1oeb

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spinqualitylabelsall models 1oeb, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

MONA/GADS SH3C DOMAIN

Overview

SH3 domains are protein recognition modules within many adaptors and, enzymes. With more than 500 SH3 domains in the human genome, binding, selectivity is a key issue in understanding the molecular basis of SH3, domain interactions. The Grb2-like adaptor protein Mona/Gads associates, stably with the T-cell receptor signal transducer SLP-76. The crystal, structure of a complex between the C-terminal SH3 domain (SH3C) of, Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide, lacks the canonical SH3 domain binding motif P-x-x-P and does not form a, frequently observed poly-proline type II helix. Instead, it adopts a, clamp-like shape around the circumfence of the SH3C beta-barrel. The, central R-x-x-K motif of the peptide forms a 3(10) helix and inserts into, a negatively ... [(full description)]

About this Structure

1OEB is a [Protein complex] structure of sequences from [Mus musculus] with CD as [ligand]. Full crystallographic information is available from [OCA].

Reference

Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76., Harkiolaki M, Lewitzky M, Gilbert RJ, Jones EY, Bourette RP, Mouchiroud G, Sondermann H, Moarefi I, Feller SM, EMBO J. 2003 Jun 2;22(11):2571-82. PMID:12773374

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